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SNAREpin assembly by Munc18-1 requires previous vesicle docking by synaptotagmin 1.

Authors: Parisotto, Daniel  Malsam, Jörg  Scheutzow, Andrea  Krause, Jean Michel  Söllner, Thomas H 
Citation: Parisotto D, etal., J Biol Chem. 2012 Sep 7;287(37):31041-9. doi: 10.1074/jbc.M112.386805. Epub 2012 Jul 18.
Pubmed: (View Article at PubMed) PMID:22810233
DOI: Full-text: DOI:10.1074/jbc.M112.386805

Regulated exocytosis requires the general membrane fusion machinery-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins. Using reconstituted giant unilamellar vesicles containing preassembled t-SNARE proteins (syntaxin 1·SNAP-25), we determined how Munc18-1 controls the docking, priming, and fusion of small unilamellar vesicles containing the v-SNARE VAMP2 and the Ca(2+) sensor synaptotagmin 1. In vitro assays allowed us to position Munc18-1 in the center of a sequential reaction cascade; vesicle docking by synaptotagmin 1 is a prerequisite for Munc18-1 to accelerate trans-SNARE complex (SNAREpin) assembly and membrane fusion. Complexin II stalls SNAREpin zippering at a late stage and, hence, contributes to synchronize membrane fusion in a Ca(2+)- and synaptotagmin 1-dependent manner. Thus, at the neuronal synapse, the priming factor Munc18-1 may accelerate the conversion of docked synaptic vesicles into a readily releasable pool by activating SNAREs for efficient membrane fusion.


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CRRD Object Information
CRRD ID: 12903989
Created: 2017-05-12
Species: All species
Last Modified: 2017-05-12
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.